ID MYO7B_HUMAN Reviewed; 2116 AA. AC Q6PIF6; Q14786; Q8TEE1; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 08-APR-2008, sequence version 2. DT 28-MAR-2018, entry version 129. DE RecName: Full=Unconventional myosin-VIIb; GN Name=MYO7B; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 166-196 (ISOFORMS 1/2). RX PubMed=8022818; DOI=10.1073/pnas.91.14.6549; RA Bement W.M., Hasson T., Wirth J.A., Cheney R.E., Mooseker M.S.; RT "Identification and overlapping expression of multiple unconventional RT myosin genes in vertebrate cell types."; RL Proc. Natl. Acad. Sci. U.S.A. 91:6549-6553(1994). RN [3] RP ERRATUM. RX PubMed=7972138; DOI=10.1073/pnas.91.24.11767c; RA Bement W.M., Hasson T., Wirth J.A., Cheney R.E., Mooseker M.S.; RL Proc. Natl. Acad. Sci. U.S.A. 91:11767-11767(1994). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1102-2116 (ISOFORM 2). RC TISSUE=Spleen; RA Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.; RT "The nucleotide sequence of a long cDNA clone isolated from human RT spleen."; RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1451-2116 (ISOFORM 1). RC TISSUE=Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION OF THE IMAC COMPLEX, RP INTERACTION WITH CDHR2; CDHR5 AND USH1C, AND REGION. RX PubMed=24725409; DOI=10.1016/j.cell.2014.01.067; RA Crawley S.W., Shifrin D.A. Jr., Grega-Larson N.E., McConnell R.E., RA Benesh A.E., Mao S., Zheng Y., Zheng Q.Y., Nam K.T., Millis B.A., RA Kachar B., Tyska M.J.; RT "Intestinal brush border assembly driven by protocadherin-based RT intermicrovillar adhesion."; RL Cell 157:433-446(2014). RN [7] RP INTERACTION WITH USH1C, AND REGION. RX PubMed=26812017; DOI=10.1016/j.devcel.2015.12.020; RA Li J., He Y., Lu Q., Zhang M.; RT "Mechanistic basis of organization of the Harmonin/USH1C-mediated RT brush border microvilli tip-link complex."; RL Dev. Cell 36:179-189(2016). RN [8] RP FUNCTION, INTERACTION WITH ANKS4B AND USH1C, AND IDENTIFICATION OF THE RP IMAC COMPLEX. RX PubMed=26812018; DOI=10.1016/j.devcel.2015.12.022; RA Crawley S.W., Weck M.L., Grega-Larson N.E., Shifrin D.A. Jr., RA Tyska M.J.; RT "ANKS4B is essential for intermicrovillar adhesion complex RT formation."; RL Dev. Cell 36:190-200(2016). CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase CC activity. Their highly divergent tails are presumed to bind to CC membranous compartments, which would be moved relative to actin CC filaments. As part of the intermicrovillar adhesion complex/IMAC CC plays a role in epithelial brush border differentiation, CC controlling microvilli organization and length. May link the CC complex to the actin core bundle of microvilli (Probable). CC {ECO:0000305|PubMed:24725409, ECO:0000305|PubMed:26812018}. CC -!- SUBUNIT: Part of the IMAC/intermicrovillar adhesion CC complex/intermicrovillar tip-link complex composed of ANKS4B, CC MYO7B, USH1C, CDHR2 and CDHR5 (PubMed:24725409, PubMed:26812018). CC Interacts with CDHR2 (PubMed:24725409). Interacts with CDHR5 CC (PubMed:24725409). Interacts with USH1C (PubMed:24725409, CC PubMed:26812017, PubMed:26812018). Interacts with ANKS4B; requires CC initial interaction with USH1C (PubMed:26812018). CC {ECO:0000269|PubMed:24725409, ECO:0000269|PubMed:26812017, CC ECO:0000269|PubMed:26812018}. CC -!- INTERACTION: CC Q9BYE9:CDHR2; NbExp=3; IntAct=EBI-4400912, EBI-493793; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cell CC projection, microvillus {ECO:0000269|PubMed:24725409}. CC Note=Enriched in the microvilli of the intestinal brush border. CC {ECO:0000269|PubMed:24725409}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q6PIF6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6PIF6-2; Sequence=VSP_032930, VSP_032931; CC Note=No experimental confirmation available.; CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase CC superfamily. Myosin family. {ECO:0000305}. CC -!- CAUTION: Represents an unconventional myosin. This protein should CC not be confused with the conventional myosin-7 (MYH7). CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH35615.2; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC010976; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; L29147; AAA20910.1; -; mRNA. DR EMBL; AK074183; BAB85009.1; -; mRNA. DR EMBL; BC035615; AAH35615.2; ALT_INIT; mRNA. DR CCDS; CCDS46405.1; -. [Q6PIF6-1] DR RefSeq; NP_001073996.1; NM_001080527.1. [Q6PIF6-1] DR UniGene; Hs.154578; -. DR PDB; 5MV7; X-ray; 2.44 A; A=1605-2116. DR PDB; 5MV8; X-ray; 1.88 A; A=1609-2116. DR PDB; 5XBF; X-ray; 1.80 A; A=1601-2116. DR PDBsum; 5MV7; -. DR PDBsum; 5MV8; -. DR PDBsum; 5XBF; -. DR ProteinModelPortal; Q6PIF6; -. DR SMR; Q6PIF6; -. DR IntAct; Q6PIF6; 3. DR STRING; 9606.ENSP00000386461; -. DR iPTMnet; Q6PIF6; -. DR PhosphoSitePlus; Q6PIF6; -. DR BioMuta; MYO7B; -. DR DMDM; 182667924; -. DR MaxQB; Q6PIF6; -. DR PaxDb; Q6PIF6; -. DR PeptideAtlas; Q6PIF6; -. DR PRIDE; Q6PIF6; -. DR Ensembl; ENST00000409816; ENSP00000386461; ENSG00000169994. [Q6PIF6-1] DR Ensembl; ENST00000428314; ENSP00000415090; ENSG00000169994. [Q6PIF6-1] DR GeneID; 4648; -. DR KEGG; hsa:4648; -. DR UCSC; uc002top.3; human. [Q6PIF6-1] DR CTD; 4648; -. DR DisGeNET; 4648; -. DR EuPathDB; HostDB:ENSG00000169994.18; -. DR GeneCards; MYO7B; -. DR H-InvDB; HIX0002437; -. DR HGNC; HGNC:7607; MYO7B. DR HPA; HPA039131; -. DR MIM; 606541; gene. DR neXtProt; NX_Q6PIF6; -. DR OpenTargets; ENSG00000169994; -. DR PharmGKB; PA31412; -. DR eggNOG; KOG4229; Eukaryota. DR eggNOG; COG5022; LUCA. DR GeneTree; ENSGT00900000140810; -. DR HOGENOM; HOG000007836; -. DR HOVERGEN; HBG052557; -. DR InParanoid; Q6PIF6; -. DR KO; K21868; -. DR OMA; KEFFTPW; -. DR OrthoDB; EOG091G00BB; -. DR PhylomeDB; Q6PIF6; -. DR TreeFam; TF335306; -. DR ChiTaRS; MYO7B; human. DR GenomeRNAi; 4648; -. DR PRO; PR:Q6PIF6; -. DR Proteomes; UP000005640; Chromosome 2. DR Bgee; ENSG00000169994; -. DR CleanEx; HS_MYO7B; -. DR ExpressionAtlas; Q6PIF6; baseline and differential. DR Genevisible; Q6PIF6; HS. DR GO; GO:0090651; C:apical cytoplasm; ISS:UniProtKB. DR GO; GO:0005903; C:brush border; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005902; C:microvillus; IDA:UniProtKB. DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW. DR GO; GO:0051015; F:actin filament binding; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008017; F:microtubule binding; IEA:InterPro. DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro. DR GO; GO:1904970; P:brush border assembly; IPI:UniProtKB. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro. DR CDD; cd14473; FERM_B-lobe; 1. DR CDD; cd01381; MYSc_Myo7; 1. DR Gene3D; 1.20.80.10; -; 2. DR Gene3D; 1.25.40.530; -; 2. DR Gene3D; 2.30.29.30; -; 2. DR Gene3D; 2.30.30.360; -; 1. DR Gene3D; 3.40.850.10; -; 3. DR InterPro; IPR019749; Band_41_domain. DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf. DR InterPro; IPR035963; FERM_2. DR InterPro; IPR019748; FERM_central. DR InterPro; IPR000299; FERM_domain. DR InterPro; IPR000048; IQ_motif_EF-hand-BS. DR InterPro; IPR036961; Kinesin_motor_dom_sf. DR InterPro; IPR001609; Myosin_head_motor_dom. DR InterPro; IPR008989; Myosin_S1_N. DR InterPro; IPR036106; MYSc_Myo7. DR InterPro; IPR000857; MyTH4_dom. DR InterPro; IPR038185; MyTH4_dom_sf. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR Pfam; PF00373; FERM_M; 1. DR Pfam; PF00612; IQ; 4. DR Pfam; PF00063; Myosin_head; 1. DR Pfam; PF00784; MyTH4; 2. DR Pfam; PF07653; SH3_2; 1. DR PRINTS; PR00193; MYOSINHEAVY. DR SMART; SM00295; B41; 2. DR SMART; SM00015; IQ; 4. DR SMART; SM00242; MYSc; 1. DR SMART; SM00139; MyTH4; 2. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF47031; SSF47031; 2. DR SUPFAM; SSF50044; SSF50044; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR SUPFAM; SSF54236; SSF54236; 2. DR PROSITE; PS50057; FERM_3; 2. DR PROSITE; PS50096; IQ; 4. DR PROSITE; PS51456; MYOSIN_MOTOR; 1. DR PROSITE; PS51016; MYTH4; 2. DR PROSITE; PS50002; SH3; 1. PE 1: Evidence at protein level; KW 3D-structure; Actin-binding; Alternative splicing; ATP-binding; KW Cell projection; Complete proteome; Cytoplasm; Cytoskeleton; KW Differentiation; Motor protein; Myosin; Nucleotide-binding; KW Phosphoprotein; Polymorphism; Reference proteome; Repeat; SH3 domain. FT CHAIN 1 2116 Unconventional myosin-VIIb. FT /FTId=PRO_0000329046. FT DOMAIN 65 760 Myosin motor. {ECO:0000255|PROSITE- FT ProRule:PRU00782}. FT DOMAIN 745 765 IQ 1. {ECO:0000255|PROSITE- FT ProRule:PRU00116}. FT DOMAIN 763 792 IQ 2. {ECO:0000255|PROSITE- FT ProRule:PRU00116}. FT DOMAIN 786 815 IQ 3. {ECO:0000255|PROSITE- FT ProRule:PRU00116}. FT DOMAIN 814 834 IQ 4. {ECO:0000255|PROSITE- FT ProRule:PRU00116}. FT DOMAIN 832 861 IQ 5. {ECO:0000255|PROSITE- FT ProRule:PRU00116}. FT DOMAIN 855 884 IQ 6. {ECO:0000255|PROSITE- FT ProRule:PRU00116}. FT DOMAIN 989 1192 MyTH4 1. {ECO:0000255|PROSITE- FT ProRule:PRU00359}. FT DOMAIN 1197 1506 FERM 1. {ECO:0000255|PROSITE- FT ProRule:PRU00084}. FT DOMAIN 1501 1567 SH3. {ECO:0000255|PROSITE- FT ProRule:PRU00192}. FT DOMAIN 1644 1793 MyTH4 2. {ECO:0000255|PROSITE- FT ProRule:PRU00359}. FT DOMAIN 1790 1896 MyTH4 3. {ECO:0000255|PROSITE- FT ProRule:PRU00359}. FT DOMAIN 1799 2102 FERM 2. {ECO:0000255|PROSITE- FT ProRule:PRU00084}. FT NP_BIND 158 165 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00782}. FT REGION 637 659 Actin-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00782}. FT REGION 916 1542 Mediates interaction with ANKS4B. FT {ECO:0000269|PubMed:24725409}. FT REGION 1501 2116 Mediates interaction with CDHR2, CDHR5 FT and USH1C. {ECO:0000269|PubMed:24725409, FT ECO:0000269|PubMed:26812017}. FT MOD_RES 904 904 Phosphoserine. FT {ECO:0000250|UniProtKB:Q99MZ6}. FT MOD_RES 1371 1371 Phosphoserine. FT {ECO:0000250|UniProtKB:Q99MZ6}. FT MOD_RES 1645 1645 Phosphoserine. FT {ECO:0000250|UniProtKB:Q99MZ6}. FT VAR_SEQ 1851 1957 ISQKEGDFFFDSLREVSDWVKKNKPQKEGAPVTLPYQVYFM FT RKLWLNISPGKDVNADTILHYHQELPKYLRGFHKCSREDAI FT HLAGLIYKAQFNNDRSQLASVPKIL -> GRAGAGQTVGGR FT AVSEALGAACGGLSLPGAPMLDQAAGTEVGGVLEQSQLHTP FT IAHAQPTPAQHPGRRRPLDQNPAGSQEDSPRKPPNFPVPSP FT SPGHQPEGGRLLL (in isoform 2). FT {ECO:0000303|Ref.4}. FT /FTId=VSP_032930. FT VAR_SEQ 1958 2116 Missing (in isoform 2). FT {ECO:0000303|Ref.4}. FT /FTId=VSP_032931. FT VARIANT 21 21 G -> S (in dbSNP:rs2404991). FT /FTId=VAR_042626. FT VARIANT 1264 1264 R -> Q (in dbSNP:rs2245408). FT /FTId=VAR_042627. FT VARIANT 1647 1647 E -> D (in dbSNP:rs13025959). FT /FTId=VAR_042628. FT VARIANT 2105 2105 Q -> R (in dbSNP:rs11686946). FT /FTId=VAR_042629. FT CONFLICT 182 182 H -> D (in Ref. 2; AAA20910). FT {ECO:0000305}. FT CONFLICT 1102 1106 LRPSL -> WSVSF (in Ref. 4; BAB85009). FT {ECO:0000305}. FT HELIX 1612 1618 {ECO:0000244|PDB:5XBF}. FT HELIX 1655 1658 {ECO:0000244|PDB:5XBF}. FT HELIX 1661 1663 {ECO:0000244|PDB:5XBF}. FT HELIX 1664 1677 {ECO:0000244|PDB:5XBF}. FT HELIX 1689 1702 {ECO:0000244|PDB:5XBF}. FT HELIX 1705 1717 {ECO:0000244|PDB:5XBF}. FT HELIX 1724 1738 {ECO:0000244|PDB:5XBF}. FT TURN 1745 1747 {ECO:0000244|PDB:5XBF}. FT HELIX 1748 1756 {ECO:0000244|PDB:5XBF}. FT TURN 1757 1760 {ECO:0000244|PDB:5XBF}. FT HELIX 1764 1777 {ECO:0000244|PDB:5XBF}. FT HELIX 1786 1793 {ECO:0000244|PDB:5XBF}. FT STRAND 1799 1805 {ECO:0000244|PDB:5XBF}. FT TURN 1806 1808 {ECO:0000244|PDB:5XBF}. FT STRAND 1809 1815 {ECO:0000244|PDB:5XBF}. FT HELIX 1821 1832 {ECO:0000244|PDB:5XBF}. FT STRAND 1840 1846 {ECO:0000244|PDB:5XBF}. FT STRAND 1849 1852 {ECO:0000244|PDB:5XBF}. FT HELIX 1859 1873 {ECO:0000244|PDB:5XBF}. FT STRAND 1886 1892 {ECO:0000244|PDB:5XBF}. FT HELIX 1904 1909 {ECO:0000244|PDB:5XBF}. FT HELIX 1911 1920 {ECO:0000244|PDB:5XBF}. FT HELIX 1928 1943 {ECO:0000244|PDB:5XBF}. FT HELIX 1947 1951 {ECO:0000244|PDB:5XBF}. FT HELIX 1953 1956 {ECO:0000244|PDB:5XBF}. FT HELIX 1957 1959 {ECO:0000244|PDB:5XBF}. FT TURN 1963 1965 {ECO:0000244|PDB:5XBF}. FT HELIX 1966 1968 {ECO:0000244|PDB:5XBF}. FT HELIX 1971 1982 {ECO:0000244|PDB:5XBF}. FT HELIX 1983 1985 {ECO:0000244|PDB:5XBF}. FT HELIX 1990 2001 {ECO:0000244|PDB:5XBF}. FT TURN 2005 2008 {ECO:0000244|PDB:5XBF}. FT STRAND 2010 2016 {ECO:0000244|PDB:5XBF}. FT STRAND 2024 2031 {ECO:0000244|PDB:5XBF}. FT STRAND 2034 2038 {ECO:0000244|PDB:5XBF}. FT TURN 2040 2042 {ECO:0000244|PDB:5XBF}. FT STRAND 2045 2049 {ECO:0000244|PDB:5XBF}. FT HELIX 2051 2053 {ECO:0000244|PDB:5XBF}. FT STRAND 2054 2059 {ECO:0000244|PDB:5XBF}. FT STRAND 2061 2068 {ECO:0000244|PDB:5XBF}. FT STRAND 2075 2080 {ECO:0000244|PDB:5XBF}. FT HELIX 2084 2099 {ECO:0000244|PDB:5XBF}. SQ SEQUENCE 2116 AA; 241599 MW; 18E908998470E4FD CRC64; MSGFRLGDHV WLEPPSTHKT GVAIGGIIKE AKPGKVLVED DEGKEHWIRA EDFGVLSPMH PNSVQGVDDM IRLGDLNEAG MVHNLLIRYQ QHKIYTYTGS ILVAVNPFQV LPLYTLEQVQ LYYSRHMGEL PPHVFAIANN CYFSMKRNKR DQCCIISGES GAGKTETTKL ILQFLATISG QHSWIEQQVL EANPILEAFG NAKTIRNDNS SRFGKYIDIY FNPSGVIEGA RIEQFLLEKS RVCRQAPEER NYHIFYCMLM GVSAEDKQLL SLGTPSEYHY LTMGNCTSCE GLNDAKDYAH IRSAMKILQF SDSESWDVIK LLAAILHLGN VGFMASVFEN LDASDVMETP AFPTVMKLLE VQHQELRDCL IKHTILIRGE FVTRSLNIAQ AADRRDAFVK GIYGHLFLWI VKKINAAIFT PPAQDPKNVR RAIGLLDIFG FENFENNSFE QLCINFANEH LQQFFVQHVF TMEQEEYRSE NISWDYIHYT DNRPTLDLLA LKPMSIISLL DEESRFPQGT DLTMLQKLNS VHANNKAFLQ PKNIHDARFG IAHFAGEVYY QAEGFLEKNR DVLSTDILTL VYSSKNKFLR EIFNLELAET KLGHGTIRQA KAGNHLFKSA DSNKRPSTLG SQFKQSLDQL MKILTNCQPY FIRCIKPNEY KKPLLFDREL CLRQLRYSGM METVHIRKSG FPIRYTFEEF SQRFGVLLPN AMRMQLQGKL RQMTLGITDV WLRTDKDWKA GKTKIFLRDH QDTLLEVQRS QVLDRAALSI QKVLRGYRYR KEFLRQRRAA VTLQAWWRGY CNRRNFKLIL VGFERLQAIA RSQPLARQYQ AMRQRTVQLQ ALCRGYLVRQ QVQAKRRAVV VIQAHARGMA ARRNFQQRKA NAPLVIPAEG QKSQGALPAK KRRSIYDTVT DTEMVEKVFG FLPAMIGGQE GQASPHFEDL ESKTQKLLEV DLDTVPMAEE PEEDVDGLAE YTFPKFAVTY FQKSASHTHI RRPLRYPLLY HEDDTDCLAA LVIWNVILRF MGDLPEPVLY ARSSQQGSSV MRQIHDTLGR EHGAQVPQHS RSAQVASQLN IGEEALEPDG LGADRPMSNL EKVHFIVGYA ILRPSLRDEI YCQICKQLSE NFKTSSLARG WILLSLCLGC FPPSERFMKY LLNFIGQGPA TYGPFCAERL RRTYANGVRA EPPTWLELQA VKSKKHIPIQ VILATGESLT VPVDSASTSR EMCMHIAHKQ GLSDHLGFSL QVAVYDKFWS LGSGRDHMMD AIARCEQMAQ ERGESQRQSP WRIYFRKEFF TPWHDSREDP VSTELIYRQV LRGVWSGEYS FEKEEELVEL LARHCYVQLG ASAESKAVQE LLPSCIPHKL YRTKPPDRWA SLVTAACAKA PYTQKQVTPL AVREQVVDAA RLQWPLLFSR LFEVITLSGP RLPKTQLILA VNWKGLCFLD QQEKMLLELS FPEVMGLATN REAQGGQRLL LSTMHEEYEF VSPSSVAIAE LVALFLEGLK ERSIFAMALQ DRKATDDTTL LAFKKGDLLV LTKKQGLLAS ENWTLGQNDR TGKTGLVPMA CLYTIPTVTK PSAQLLSLLA MSPEKRKLAA QEGQFTEPRP EEPPKEKLHT LEEFSYEFFR APEKDMVSMA VLPLARARGH LWAYSCEPLR QPLLKRVHAN VDLWDIACQI FVAILRYMGD YPSRQAWPTL ELTDQIFTLA LQHPALQDEV YCQILKQLTH NSNRHSEERG WQLLWLCTGL FPPSKGLLPH AQKFIDTRRG KLLAPDCSRR IQKVLRTGPR KQPPHQVEVE AAEQNVSRIC HKIYFPNDTS EMLEVVANTR VRDVCDSIAT RLQLASWEGC SLFIKISDKV ISQKEGDFFF DSLREVSDWV KKNKPQKEGA PVTLPYQVYF MRKLWLNISP GKDVNADTIL HYHQELPKYL RGFHKCSRED AIHLAGLIYK AQFNNDRSQL ASVPKILREL VPENLTRLMS SEEWKKSILL AYDKHKDKTV EEAKVAFLKW ICRWPTFGSA FFEVKQTSEP SYPDVILIAI NRHGVLLIHP KTKDLLTTYP FTKISSWSSG STYFHMALGS LGRGSRLLCE TSLGYKMDDL LTSYVQQLLS AMNKQRGSKA PALAST //